Abstract:
:This study describes for the first time the amphiphilicity of the protein moiety of proteoglycogen. Glycogenin but not proteoglycogen associates to phospholipid vesicles and forms by itself stable Gibbs and Langmuir monolayers at the air-buffer interface. The adsorption free energy (-6.7 kcal/mol) and the glycogenin collapse pressure (47 mN/m) are indicative of its high surface activity which can thermodynamically drive and retain the protein at the membrane interface to a maximum equilibrium adsorption surface pressure of 21 mN/m. The marked surface activity of glycogenin is further enhanced by its thermodynamically favorable penetration into zwitterionic and anionic phospholipids with a high cut-off surface pressure point above 30 mN/m. The strong association to phospholipid vesicles and the marked surface activity of glycogenin correspond to a high amphiphilic character which supports its spontaneous association to membrane interfaces, in which the de novo biosynthesis of glycogen was proposed to initiate.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Carrizo ME,Miozzo MC,Maggio B,Curtino JAdoi
10.1016/s0014-5793(01)03192-1keywords:
subject
Has Abstractpub_date
2001-12-07 00:00:00pages
323-6issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(01)03192-1journal_volume
509pub_type
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